EC Number |
General Information |
Reference |
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2.6.1.78 | malfunction |
one PAT incompetent 1beta AAT mutant K12G from Rhizobium meliloti is detected (UniProt ID P58350) |
759178 |
2.6.1.78 | metabolism |
the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview |
-, 759178 |
2.6.1.78 | more |
key residues, such as Glu108, are involved in both keto acid and amino acid substrate specificities and probably contribute to the evolution of PAT activity among class Ibeta AAT enzymes, ligand binding study, molecular mechanisms underlying recognition of keto acid and amino acid substrates, overview. Lys306 is the catalytic Lys in AtPAT |
759965 |
2.6.1.78 | more |
modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview |
-, 759178 |
2.6.1.78 | more |
modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview. Lys12 plays a specific role in prephenate binding by PAT competent 1beta AAT |
759178 |
2.6.1.78 | physiological function |
suppression of prephenate aminotransferase leads to a severe reduction in growth and strong chlorosis symptoms. Prephenate aminotransferase silenced plants exhibit extremely reduced levels of asparagine and are greatly affected in their phenylalanine metabolism and lignin deposition. Prephenate aminotransferase suppression triggers a transcriptional reprogramming in plastid nitrogen metabolism. The enzyme is essential for plant growth and development |
739351 |